(Z,4S,5R)-2-azaniumyl-4,5,6-trihydroxyhex-2-enoate

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: (Z,4S,5R)-2-azaniumyl-4,5,6-trihydroxyhex-2-enoate
• 化学式: C6H11NO5
• 分子量: 177.16
• InChiKey: BWCRWWBHRAOURT-VYOXQMNSSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.4
• 重原子数：
  12
• 可旋转键数：
  4
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  124
• 氢给体数：
  5
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  (Z,4S,5R)-2-azaniumyl-4,5,6-trihydroxyhex-2-enoate 生成 (4S,5R)-4,5,6-trihydroxy-2-iminohexanoic acid
  参考文献：
  名称：

  D-Glucosaminate Dehydratase from Agrobacterium radiobacter. Physicochemical and Enzymological Properties

  摘要：

  研究了 D-氨基葡萄糖脱水酶 EEC 4.2.1.26]的细菌分布情况，发现辐射农杆菌（IAM 1526）的酶活性最高。在甘油-尿素培养基中，D-氨基葡萄糖、D-半乳糖胺和 D-氨基葡萄糖可诱导形成该酶，但 D-甘露糖胺不能诱导形成该酶。通过超速离心法，从葡萄糖胺-甘油-尿素培养基中生长的细胞中纯化出的酶是均匀的。用沉降平衡法测定其分子量约为 66 000，用凝胶渗透色谱低角度光散射法测定其分子量约为 72 800。最适 pH 值为 8.3-9.0。该酶可催化 D-氨基葡萄糖酸（相对活性：100，Km：2.8 mM）、D-半乳糖氨酸（31.5，5.0 mM）、D-甘露氨酸（17.5，29 mM）、D-苏氨酸（5.1，4.8 mM）、D-丝氨酸（3.2，0.026 mM）和 L-丝氨酸（1.1，ND）脱水，但不能催化 L-苏氨酸。反向反应不会发生。该酶受 5'-磷酸吡哆醛酶的典型抑制剂（如 L-青霉胺）以及羰基试剂、硫醇试剂、二价金属和几种 D-氨基酸和 D-氨基糖的抑制。

  DOI：

  10.1093/oxfordjournals.jbchem.a133686
• 作为产物：
  描述：

  D-氨基葡萄糖酸 生成 (Z,4S,5R)-2-azaniumyl-4,5,6-trihydroxyhex-2-enoate 、 水
  参考文献：
  名称：

  D-Glucosaminate Dehydratase from Agrobacterium radiobacter. Physicochemical and Enzymological Properties

  摘要：

  研究了 D-氨基葡萄糖脱水酶 EEC 4.2.1.26]的细菌分布情况，发现辐射农杆菌（IAM 1526）的酶活性最高。在甘油-尿素培养基中，D-氨基葡萄糖、D-半乳糖胺和 D-氨基葡萄糖可诱导形成该酶，但 D-甘露糖胺不能诱导形成该酶。通过超速离心法，从葡萄糖胺-甘油-尿素培养基中生长的细胞中纯化出的酶是均匀的。用沉降平衡法测定其分子量约为 66 000，用凝胶渗透色谱低角度光散射法测定其分子量约为 72 800。最适 pH 值为 8.3-9.0。该酶可催化 D-氨基葡萄糖酸（相对活性：100，Km：2.8 mM）、D-半乳糖氨酸（31.5，5.0 mM）、D-甘露氨酸（17.5，29 mM）、D-苏氨酸（5.1，4.8 mM）、D-丝氨酸（3.2，0.026 mM）和 L-丝氨酸（1.1，ND）脱水，但不能催化 L-苏氨酸。反向反应不会发生。该酶受 5'-磷酸吡哆醛酶的典型抑制剂（如 L-青霉胺）以及羰基试剂、硫醇试剂、二价金属和几种 D-氨基酸和 D-氨基糖的抑制。

  DOI：

  10.1093/oxfordjournals.jbchem.a133686

文献信息

• D-Glucosaminate Dehydratase from Agrobacterium radiobacter. Physicochemical and Enzymological Properties
  作者：Ryoko IWAMOTO、Yujiro IMANAGA、Kenji SODA

  DOI：10.1093/oxfordjournals.jbchem.a133686

  日期：1982.1

  The bacterial distribution of D-glucosaminate dehydratase EEC 4.2.1.26] was investigated and Agrobacterium radiobacter (IAM 1526) was found to have the highest enzyme activity. The enzyme was formed inducibly in a glycerol-urea medium by D-glucosaminate, D-galactosamine, and D-glucosamine, but not by D-mannosamine. The enzyme purified from the cells grown in the glucosamine-glycerol-urea medium was shown to be homogeneous by ultracentrifugation. The molecular weight was determined to be about 66,000 by the sedimentation equilibrium method, and 72,800 by the gel permeation chromatography low-angle light scattering method. The pH optimum is 8.3–9.0. The enzyme catalyzed the dehydration of D-glucosaminate (relative activity: 100, Km: 2.8 mM), D-galactosaminate (31.5, 5.0 mM), D-manno saminate (17.5, 29 mM), D-threonifle (5.1, 4.8 mM), D-serine (3.2, 0.026 mM), and L-serine (1.1, ND), but not L-threonine. The reverse reaction does not occur. The enzyme is inhibited by typical inhibitors of pyridoxal 5'-phosphate enzymes, such as L-penicillamine, and also by carbonyl reagents, thiol reagents, divalent metals, and several D-amino acids and D-amino sugars.

  研究了 D-氨基葡萄糖脱水酶 EEC 4.2.1.26]的细菌分布情况，发现辐射农杆菌（IAM 1526）的酶活性最高。在甘油-尿素培养基中，D-氨基葡萄糖、D-半乳糖胺和 D-氨基葡萄糖可诱导形成该酶，但 D-甘露糖胺不能诱导形成该酶。通过超速离心法，从葡萄糖胺-甘油-尿素培养基中生长的细胞中纯化出的酶是均匀的。用沉降平衡法测定其分子量约为 66 000，用凝胶渗透色谱低角度光散射法测定其分子量约为 72 800。最适 pH 值为 8.3-9.0。该酶可催化 D-氨基葡萄糖酸（相对活性：100，Km：2.8 mM）、D-半乳糖氨酸（31.5，5.0 mM）、D-甘露氨酸（17.5，29 mM）、D-苏氨酸（5.1，4.8 mM）、D-丝氨酸（3.2，0.026 mM）和 L-丝氨酸（1.1，ND）脱水，但不能催化 L-苏氨酸。反向反应不会发生。该酶受 5'-磷酸吡哆醛酶的典型抑制剂（如 L-青霉胺）以及羰基试剂、硫醇试剂、二价金属和几种 D-氨基酸和 D-氨基糖的抑制。
• <scp>D</scp>-Glucosaminate Aldolase Activity of<scp>D</scp>-Glucosaminate Dehydratase from<i>Pseudomonas fluorescens</i>and Its Requirement for Mn²⁺Ion
  作者：Ryoko Iwamoto、Hisae Taniki、Junko Koishi、Satomi Nakura

  DOI：10.1271/bbb.59.408

  日期：1995.1

  When D-glucosaminate dehydratase (GADH) was incubated with D-glucosaminate (GlcNA) in veronal buffer (VB; 0.01 M, pH 8.0), GlcNA was converted stoichiometrically to glyceraldehyde, pyruvate, and ammonia (aldolase reaction A). This reaction occurred in addition to the dehydratase reaction (conversion of GlcNA to 2-keto-3-deoxy-o-gluconate and ammonia: α,β-elimination reaction, B). The ratio of the activities (A:B) was about 1:4. However, in potassium phosphate buffer (KPB; 0.04 M, pH 8.0), the aldolase reaction was inhibited to 3–4% of that in VB, and also inhibited by various derivatives of glycerol, in particular, glycerol-3-phosphate (glycerol-3-P) and glyceraldehyde-3-phosphate (glyceraldehyde-3-P) in VB. The native enzyme was inhibited by incubation with 0.1 M EDTA, and the activity was restored by incubation of the EDTA-treated enzyme with (Mn2+ + pyridoxal 5′-phosphate (PLP)). When the EDTA-treated enzyme was incubated with (Mn2+ + PLP + glycerol-3-P), the activity of reaction B increased to 131% but that of reaction A decreased to 21%. These results suggested that Mn2+, PLP, and the phosphate group of glycerol-3-P are involved in formation of the active enzyme. In the case of the aldolase reaction, Mn2+ ion, which might be essential for the reaction, is chelated by the phosphate group of glycerol-3-P with resultant inhibition of the aldolase reaction.

  当D-氨基葡萄糖酸脱氢酶（GADH）与D-氨基葡萄糖酸（GlcNA）在维罗纳缓冲液（VB；0.01 M，pH 8.0）中孵育时，GlcNA按化学计量转化为甘油醛、丙酮酸和氨（醛缩酶反应A）。除了脱氢酶反应（将GlcNA转化为2-酮-3-脱氧-o-葡萄糖酸和氨：α，β-消除反应，B）外，还会发生这种反应。活性比（A：B）约为1：4。然而，在磷酸钾缓冲液（KPB；0.04 M，pH 8.0）中，醛缩酶反应被抑制至VB反应的3-4%，并且被甘油的各种衍生物抑制，特别是VB中的甘油-3-磷酸（甘油-3-P）和甘油醛-3-磷酸（甘油醛-3-P）。天然酶在0.1 M EDTA中孵育会被抑制，而经EDTA处理的酶在（Mn2+ +吡哆醛5′-磷酸（PLP））中孵育后活性会恢复。当经EDTA处理的酶在（Mn2+ + PLP +甘油-3-P）中孵育时，反应B的活性会增加到131%，但反应A的
• The d-glucosaminate dehydratase alpha-subunit from Pseudomonas fluorescens exhibits thioredoxin reductase activity
  作者：Ryoko Iwamoto、Chie Amano、Kenji Ikehara、Naomi Ushida

  DOI：10.1016/s1570-9639(03)00079-7

  日期：2003.4

  The complete amino acid sequence of the D-glucosaminate dehydratase (GADH) alpha-subunit from Pseudomonas fluorescens was determined by PCR using genomic DNA from P fluorescens as a template. The alpha-subunit comprises 320 amino acids and has a molecular mass of about 33.9 kDa. The primary structure of the alpha-subunit demonstrates a high similarity to the structures of thioredoxin reductase (TrxR) from many prokaryotes, especially Pseudomonas aeruginosa (identity 85%, positive 91%), Vibrio cholerae (identity 73%, positive 85%), and Escherichia coli (identity 71%, positive 83%). The purified glucosaminate dehydratase alpha(2)-enzyme exhibited NADPH-dependent TrxR activity, while TrxR from E. coli showed pyridoxal 5'-phosphate (PLP)-dependent GADH activity. The TrxR from E. coli suggests that there are three cofactor binding sites, FAD, NADPH, and PLP in the enzyme and that TrxR catalyzes the FAD- and NADPH-dependent oxidation-reduction reaction and the PLP-dependent alpha,beta-elimination reaction. (C) 2003 Elsevier Science B.V. All rights reserved.